[Structural-functional UV-modifications of C1q factor of the human complement system].
The structural transformations of C1q-protein induced by the UV-light at doses 151 and 2265 J/m2 has been determined by means of acid-basic titration, IR- ans UV-spectrophotometry. These transformations are stipulated by unfolding of its molecules without change of the secondary structure types ratio and accompanies by exposition on aromatic amino acid residues as well as glutamine and asparagine acids, lysine, hydroxylysine and cysteine on the globule surface. The correlation between structural photomodifications and processes of functional activation of C1q has been established.
Gusinskaia
V V
VV
Voronezh State University, Russia.
Artiukhov
V G
VG
Sergeev
K P
KP
D000596:Amino Acids / Q000032:analysis; D001216:Asparagine / Q000032:analysis; D015922:Complement C1q / Q000378:metabolism / Q000502:physiology / Q000528:radiation effects*; D003545:Cysteine / Q000032:analysis; D005973:Glutamine / Q000032:analysis; D006801:Humans; D006901:Hydroxylysine / Q000032:analysis; D008239:Lysine / Q000032:analysis; D018448:Models, Immunological; D013055:Spectrophotometry, Infrared; D013056:Spectrophotometry, Ultraviolet; D014466:Ultraviolet Rays
D000596:Amino Acids; D005973:Glutamine; D006901:Hydroxylysine; D001216:Asparagine; D015922:Complement C1q; D008239:Lysine; D003545:Cysteine
Strukturno-funktsional'nye UF-modifikatsii C1q-faktora sistemy komplementa cheloveka.